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  • 2000-2004  (2)
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Material
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  • 1
    Electronic Resource
    Electronic Resource
    Structure of human erythrocyte catalase (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 241-245 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P212121 and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 Å, was determined and refined with 2.75 Å resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and Rfree were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999015930
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of tetragonal crystals of human erythrocyte catalase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1-7 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I41 by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6 Å, yielding R and Rfree of 0.196 and 0.244, respectively, for all data at 2.4 Å resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4122 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900013767
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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